Journal
CHEMBIOCHEM
Volume 9, Issue 3, Pages 420-425Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200700450
Keywords
cytochromes; epoxidation; monooxygenases; Sulfolobus acidocaldarius; thermostability
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We report the cloning, expression, and purification of CYP119, a thermostable enzyme previously thought to derive from Sulfolobus solfataricus. Sequence analysis suggested that, in contrast to the conclusions of earlier studies, the enzyme stems from the closely related Sulfolobus acidocaldarius, and we were indeed able to clone the gene from the genomic DNA of this organism. For the first time, we report here on the peroxidase activity of this enzyme and the optimization of the associated reaction parameters. The optimized reaction conditions were then applied to the biocotalytic epoxidation of styrene. The values obtained for k(cat) (78.2 +/- 20.6 min(-1)) and K-M (9.2 +/- 4.3 mm) indicated an approximately 100-fold increased catalytic activity over previously reported results.
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